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2 tion demonstrated that FIA-ESI-HRMS (MSX and FTMS) is applicable for quantification of FC and CE in s
5 m/z values below 1000 have been observed by FTMS of whole cells, this represents the first report of
7 is - Fourier transform mass spectrometry (CE-FTMS) and showed a differential metabolic separation bet
8 cidated using HPLC ESI capillary-skimmer CID FTMS by correlating their fragmentation patterns with th
10 ially increases the capabilities of top down FTMS for the detailed structural characterization of lar
14 igonucleotide products is mass mapped by ESI-FTMS analysis, which enables the unambiguous identificat
15 eated with ribonucleases and analyzed by ESI-FTMS to obtain the correct position of chemically modifi
17 extracted, digested, and analyzed by LC-ESI-FTMS/MS to find highly conserved peptides as markers of
20 ion-Fourier transform mass spectrometry (ESI-FTMS) is employed in place of polyacrylamide gel electro
25 oteins have been detected directly using ESI-FTMS (or MALDI-TOF), and the fractionation showed a peak
27 haracteristic is particularly beneficial for FTMS applications in which a sharp reduction of metastab
28 ight species presents a unique challenge for FTMS, as a result not only of the high cyclotron frequen
30 This information is also accessible from FTMS mass spectra obtained in commonly used workflows di
31 s a control, accurate mass measurements from FTMS and collision-induced dissociation spectra, 11 nove
33 mprehensive analysis approach based on HILIC-FTMS was developed to concurrently examine polar metabol
34 e MeOH/ACN/Acetone extraction with the HILIC-FTMS method for metabolite profiling and smoking-related
37 d, namely, accurate mass fragmentation (HPLC-FTMS(n)) and mass-guided SPE-trapping of selected compou
45 btained by analogous electrospray ionization-FTMS experiments, with no evidence of either metastable
48 tion of thousands of peptides in a single LC-FTMS analysis by comparing accurate molecular mass and L
52 ddition, the performance of the new HP-MALDI FTMS configuration and its potential application for hig
54 n Fourier transform mass spectrometry (MALDI FTMS) for neuropeptide analysis of complex tissue sample
66 tics of crustacean neuropeptides under MALDI-FTMS conditions and show how fragments formed by Asp-Xxx
69 d that, upon full scan Fourier transform MS (FTMS) quantification, CE species show substantial differ
72 exceptional m/ z resolution and accuracy of FTMS are indispensable for frontline biological and envi
73 n encrypted in DOM and assess the quality of FTMS-derived molecular formulas of complex mixtures in g
75 sor ion scanning, higher resolution scans on FTMS instruments, and improved peptide quantitation.
76 meter (advanced quadrupole filter, optimized FTMS scan overhead) and new instrument control software
77 ly can be realized using high-field Orbitrap FTMS and/or future generation of ultrahigh magnetic fiel
78 spite being initially developed for Orbitrap FTMS, the method is likewise applicable for ion cyclotro
82 h, estuarine DOM samples were analyzed by OT-FTMS coupled to IC in negative mode and LC in positive m
84 rbitrap Fusion Tribrid mass spectrometer (OT-FTMS), which assures high mass accuracy at every scan by
85 ntly below 1.0 ppm mass error, giving the OT-FTMS the potential of reaching mass accuracy of the Four
87 e I (42 kDa) yielded as many as 70 peptides, FTMS identification of the labeled peptide localized the
88 raw MS/MS data (obtained using a quadrupole-FTMS hybrid instrument) for one protein that differed fr
89 e to the poor performance of high-resolution FTMS for the analysis of larger proteoforms and the high
93 ch as a Fourier transform mass spectrometer (FTMS) allows accumulation of ions in the cell from m
94 source Fourier transform mass spectrometer (FTMS) equipped with matrix-assisted laser desorption/ion
95 n (ESI) Fourier transform mass spectrometer (FTMS) to characterize nucleic acid substrates modified b
96 eved by Fourier transform mass spectrometry (FTMS) allowed for the incorporation of substrates with s
97 solving Fourier Transform mass spectrometry (FTMS) allows to distinguish between most isobaric compou
100 m ion cyclotron resonance mass spectrometry (FTMS) has been applied to the direct analysis of crustac
101 ed with Fourier transform mass spectrometry (FTMS) has proven to be a useful technique for the studie
102 olution Fourier transform mass spectrometry (FTMS) has revealed unprecedented details of natural comp
103 nces in Fourier transform mass spectrometry (FTMS) instrumentation, top-down proteomics (TDP) is curr
104 ccuracy Fourier transform mass spectrometry (FTMS) is becoming increasingly attractive due to its spe
105 I) with Fourier transform mass spectrometry (FTMS) is described, and its significance for the high-re
106 henated Fourier transform mass spectrometry (FTMS) methods affords additional information about compl
107 tion of Fourier transform mass spectrometry (FTMS) to analysis of bacterial proteins directly from wh
108 n (ESI) Fourier transform mass spectrometry (FTMS) to assess the ability of a series of nucleic acid
110 (SPLC), Fourier transform mass spectrometry (FTMS), data-independent acquisition (DIA) with nozzle-sk
120 the high-performance data acquisition system FTMS Booster X2 provided access to the unreduced data in
121 n using an external data acquisition system, FTMS Booster X2, coupled to a Q Exactive HF Orbitrap FTM
129 aneous detection of molecular hydrogen using FTMS and demonstrate the experimental conditions necessa
131 a 1.7 mm cryo-microprobe in combination with FTMS, exciton coupled CD, and stereochemical correlation
132 coupling of laser desorption techniques with FTMS was realized two decades ago, several different sol